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Chemerin Receptors CMKLR1 (Chemerin1) and GPR1 (Chemerin2) Nomenclature, Pharmacology, and Function

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Chemerin Receptors CMKLR1 (Chemerin1) and GPR1 (Chemerin2) Nomenclature, Pharmacology, and Function 1521-0081/70/1/174–196$25.00 https://doi.org/10.1124/pr.116.013177 PHARMACOLOGICAL REVIEWS Pharmacol Rev 70:174–196, January 2018 Copyright © 2017 by The Author(s) This is an open access article distributed under the CC BY Attribution 4.0 International license. ASSOCIATE EDITOR: ELIOT H. OHLSTEIN International Union of Basic and Clinical Pharmacology CIII: Chemerin Receptors CMKLR1 (Chemerin1) and GPR1 (Chemerin2) Nomenclature, Pharmacology, and Function Amanda J. Kennedy and Anthony P. Davenport Experimental Medicine and Immunotherapeutics, University of Cambridge, Centre for Clinical Investigation, Addenbrooke’s Hospital, Cambridge, United Kingdom Abstract ...................................................................................175 I. Introduction . ..............................................................................175 II. Chemokine-Like Receptor 1 Designated as Chemerin Receptor 1 . .........................177 III. G Protein–Coupled Receptor 1 Designated as Chemerin Receptor 2 .........................177 IV. Distribution . ..............................................................................179 Downloaded from A. Chemerin Receptor 1 . ..................................................................179 1. Humans ............................................................................179 2. Mice . ..............................................................................179 3. Rats . ..............................................................................179 4. Other Species .......................................................................179 by guest on September 23, 2021 B. Chemerin Receptor 2 . ..................................................................180 1. Humans ............................................................................180 2. Mice . ..............................................................................181 3. Rats . ..............................................................................181 4. Other Species .......................................................................181 C. Chemerin ..............................................................................181 1. Humans ............................................................................181 2. Mice . ..............................................................................183 3. Rats . ..............................................................................183 4. Other Species .......................................................................183 V. Radiolabeled Ligands ......................................................................183 VI. Agonists ...................................................................................185 A. Chemerin Receptor 1 Agonists..........................................................185 B. Chemerin Receptor 2 Agonists..........................................................187 VII. Antagonists. ..............................................................................187 VIII. Receptor Signaling. ........................................................................188 A. Signaling Pathways Activated by Chemerin Receptor 1 . ...............................188 B. Signaling Pathways Activated by Chemerin Receptor 2 . ...............................189 IX. Physiologic Roles . ........................................................................189 A. Chemerin Receptor 1 . ..................................................................189 1. Immunity. ........................................................................189 2. Antibacterial/Antimicrobial Agent . ................................................189 3. Adipogenesis and Energy Metabolism ...............................................190 4. Cardiovascular System. ............................................................190 B. Chemerin Receptor 2 . ..................................................................190 This work was supported by the British Heart Foundation [FS/12/64/30001 to A.J.K.] and Wellcome Trust [WT107715/Z/15/Z]. Address correspondence to: Dr. Anthony P. Davenport, Experimental Medicine and Immunotherapeutics, University of Cambridge, Level 6, Addenbrooke’s Centre For Clinical Investigation, Box 110, Addenbrooke’s Hospital, CB2 0QQ Cambridge, UK. E-mail: apd10@ medschl.cam.ac.uk https://doi.org/10.1124/pr.116.013177. 174 Chemerin Receptor (Chemerin1 and Chemerin2) Nomenclature 175 X. Pathophysiological Roles . ..................................................................190 A. Chemerin Receptor 1 . ..................................................................190 1. Inflammation .......................................................................190 2. Obesity .............................................................................191 3. Cardiovascular Disease . ............................................................191 4. Other Roles. ........................................................................191 B. Chemerin Receptor 2 . ..................................................................192 1. Human Immunodeficiency Virus ....................................................192 2. Other Roles. ........................................................................192 XI. Genetically Modified Animals . ............................................................192 A. Chemerin Receptor 1 . ..................................................................192 B. Chemerin Receptor 2 . ..................................................................193 References . ..............................................................................193 Abstract——Chemerin, a chemoattractant protein C-terminal processing for activity, and human and adipokine, has been identified as the endogenous chemerin21–157 is reported to be the most active ligand for a G protein–coupled receptor encoded by the form, with peptide fragments derived from the C gene CMKLR1 (also known as ChemR23), and as a terminus biologically active at both receptors. Small- consequence the receptor protein was renamed the molecule antagonist, CCX832, selectively blocks chemerin receptor in 2013. Since then, chemerin has CMKLR1, and resolvin E1 activation of CMKLR1 is been identified as the endogenous ligand for a second G discussed. Activation of both receptors by chemerin is protein–coupled receptor, encoded by the gene GPR1. via coupling to Gi/o, causing inhibition of adenylyl Therefore, the International Union of Basic and Clinical cyclase and increased Ca2+ flux. Receptors and ligand Pharmacology Committee on Receptor Nomenclature are widely expressed in humans, rats, and mice, and and Drug Classification recommends that the official both receptors share ∼80% identity across these species. name of the receptor protein for chemokine-like CMKLR1 knockout mice highlight the role of this receptor 1 (CMKLR1) is chemerin receptor 1, and G receptor in inflammation and obesity, and similarly, protein–coupled receptor 1 is chemerin receptor 2 to GPR1 knockout mice exhibit glucose intolerance. In follow the convention of naming the receptor protein addition, the chemerin receptors have been implicated after the endogenous ligand. Chemerin receptor 1 and in cardiovascular disease, cancer, steroidogenesis, chemerin receptor 2 can be abbreviated to Chemerin1 human immunodeficiency virus replication, and and Chemerin2, respectively. Chemerin requires neurogenerative disease. I. Introduction of the signal peptide, circulates in the plasma and has low biologic activity; it needs to be further processed at the C Chemerin, the endogenous ligand of chemokine-like receptor 1 (CMKLR1) or ChemR23, was identified in terminus to give the active form (Meder et al., 2003; 2003 as the product of the RARRES2 gene (Meder et al., Wittamer et al., 2003; Zabel et al., 2005a,b; Cash et al., 2003; Wittamer et al., 2003). In 1997, the RARRES2 gene 2008; Du et al., 2009; Ernst and Sinal, 2010). More detailed – was first identified as a novel retinoid-responsive gene in reviews are listed in Table 1. Human chemerin21 157 is psoriatic skin lesions (Nagpal et al., 1997). As a conse- reported to be the most active form; removal of one amino quence of its production in response to retinoid substances, acid (chemerin21–156) resulted in a sixfold drop in potency, the gene product was initially christened as tazarotene- whereas the addition of one or removal of two or three induced gene 2 (TIG2) or retinoic acid receptor responder amino acids strongly affected potency, with no response 2 protein (RARRES2). The human gene translates into a seen up to 10 mM (Wittamer et al., 2004). The C terminus is 163-amino-acid protein (mol. wt. 18,618 Da), made up of a therefore very important for function at CMKLR1, exem- 20-amino-acid hydrophobic N-terminal signal peptide, an plified further by synthetic C-terminal fragments of human intervening 137-amino-acid cystatin-fold containing chemerin: C9 (or chemerin-9), chemerin149–157; C13, domain, and a six-amino-acid C-terminal prosegment chemerin145–157 (Wittamer et al., 2004); and C20, chem- (Fig. 1A). Amino acids 21–157, corresponding to the erin138–157 (Li et al., 2014a), possessing biologic activity 137-amino-acid intervening region, were found to be the (Fig. 1C). It is not yet known whether these short peptides active part of the protein and subsequently named chem- are generated endogenously. erin (Wittamer et al., 2003). Prochemerin, the 143-amino- In addition to activating CMKLR1, human chem-
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